Generation of potential structures for the G-domain of chloroplast EF-Tu using comparative molecular modeling.
Comparative molecular modeling has been used to generate several possible structures for the G-domain of chloroplast elongation factor Tu (EF-Tu(chl)) based on the crystallographic data of the homologous E. coli protein. EF-Tu(chl) contains a 10 amino acid insertion not present in the E. coli protein and this region has been modeled based on its predicted secondary structure. The insertion appears to lie on the surface of the protein. Its orientation could not be determined unequivocally but several likely structures for the nucleotide binding domain of EF-Tu(chl) have been developed. The effects of the presence of water in the Mg2+ coordination sphere and of the protonation state of the GDP ligand on the conformation of the guanine nucleotide binding site have been examined. Relative binding constants of several guanine nucleotide analogs for EF-Tu(chl) have been obtained. The interactions between EF-Tu(chl) and GDP predicted to be important by the models that have been developed are discussed in relation to the nucleotide binding properties of this factor and to the interactions proposed to be important in the binding of guanine nucleotides to related proteins.
Lapadat
M A
MA
Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290.
Deerfield
D W
DW
Pedersen
L G
LG
Spremulli
L L
LL
D002736:Chloroplasts; D006153:Guanosine Diphosphate / Q000378:metabolism; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
D014867:Water; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu; D008274:Magnesium